ID   CHB_VIBHA               Reviewed;         883 AA.
AC   P13670;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=N,N'-diacetylchitobiase;
DE            Short=Chitobiase;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase;
DE   AltName: Full=N-acetyl-beta-glucosaminidase;
DE   Flags: Precursor;
GN   Name=chb;
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DIACYLGLYCEROL AT CYS-18.
RX   PubMed=2670926; DOI=10.1016/s0021-9258(18)63767-6;
RA   Soto-Gil R.W., Zysking J.W.;
RT   "N,N'-diacetylchitobiase of Vibrio harveyi. Primary structure, processing,
RT   and evolutionary relationships.";
RL   J. Biol. Chem. 264:14778-14783(1989).
CC   -!- FUNCTION: Hydrolysis of terminal, non-reducing N-acetyl-beta-D-
CC       glucosamine residues in chitobiose and higher analogs, and in
CC       glycoproteins.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC   -!- PATHWAY: Glycan degradation; chitin degradation.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.
CC   -!- INDUCTION: By chitobiose.
CC   -!- PTM: This protein is probably a lipoprotein, its processing is
CC       inhibited by globomycin.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family. {ECO:0000305}.
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DR   EMBL; J05004; AAA88682.1; -; Genomic_DNA.
DR   PIR; A36511; A36511.
DR   AlphaFoldDB; P13670; -.
DR   SMR; P13670; -.
DR   STRING; 669.AL538_13335; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   PRIDE; P13670; -.
DR   UniPathway; UPA00349; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd02847; E_set_Chitobiase_C; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 3.30.379.10; -; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004866; CHB/HEX_N_dom.
DR   InterPro; IPR004867; CHB_C_dom.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR015882; HEX_bac_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR22600; PTHR22600; 1.
DR   Pfam; PF03173; CHB_HEX; 1.
DR   Pfam; PF03174; CHB_HEX_C; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SMART; SM01081; CHB_HEX; 1.
DR   SUPFAM; SSF49384; SSF49384; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF55545; SSF55545; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cell outer membrane; Chitin degradation;
KW   Disulfide bond; Glycosidase; Hydrolase; Lipoprotein; Membrane; Palmitate;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..17
FT   CHAIN           18..883
FT                   /note="N,N'-diacetylchitobiase"
FT                   /id="PRO_0000012019"
FT   ACT_SITE        537
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   LIPID           18
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           18
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|PubMed:2670926"
FT   DISULFID        54..64
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..402
FT                   /evidence="ECO:0000250"
FT   DISULFID        502..577
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   883 AA;  97771 MW;  8ED14598B1FEEBCE CRC64;
     MLKHSLIAAS VITTLAGCSS LQSSEQQVVN SLADNLDIQY EVLTNHGANE GLACQDMGAE
     WASCNKVNMT LVNQGEAVDS KDWAIYFHSI RLILDVDNEQ FKISRVTGDL HKLEPTDKFD
     GFAAGEEVVL PLVGEYWQLF ETDFMPGAFV SAPNAEPKMI ASLNTEDVAS FVTGLEGNNL
     KRTPDDNNVF ANAVSRFEKN EDLATQDVST TLLPTPMHVE AGKGKVDIAD GIALPKDAFD
     ATQFAAIQDR AEVVGVDVRG DLPVSITVVP ADFTGELAKS GAYEMSIKGD GIVIKAFDQA
     GAFYAVQSIF GLVDSQNADS LPQLSIKDAP RFDYRGVMVD VARNFHSKDA ILATLDQMAA
     YKMNKLHLHL TDDEGWRLEI PGLPELTEVG ANRCFDTQEK SCLLPQLGSG PTTDNFGSGY
     FSKADYVEIL KYAKARNIEV IPEIDMPAHA RAAVVSMEAR YDRLMEEGKE AEANEYRLMD
     PQDTSNVTTV QFYNKQSFIN PCMESSTRFV DKVISEVAAM HQEAGAPLTT WHFGGDEAKN
     IKLGAGFQDV NAEDKVSWKG TIDLSKQDKP FAQSPQCQTL ITDGTVSDFA HLPSHFAEEV
     SKIVAEKGIP NFQAWQDGLK YSDGEKAFAT ENTRVNFWDV LYWGGTSSVY EWSKKGYDVI
     VSNPDYVYMD MPYEVDPKER GYYWATRATD TRKMFGFAPE NMPQNAETSV DRDGNGFTGK
     GEIEAKPFYG LSAQLWSETV RNDEQYEYMV FPRVLAAAQR AWHRADWEND YKVGVEYSQN
     SNLVDKASLN QDYNRFANVL GQRELAKLEK SGIDYRLPVP GAKVEDGKLA MNVQFPGVTL
     QYSLDGENWL TYADNARPNV TGEVFIRSVS ATGEKVSRIT SVK